bifunctional 2-methylcitrate synthase/citrate synthase

LOCUS       WP_007464609             390 aa            linear   BCT 25-FEB-2025
            [Photobacterium marinum].
ACCESSION   WP_007464609
VERSION     WP_007464609.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium marinum
  ORGANISM  Photobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF009006.1
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK12351
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Photobacterium marinum"
                     /db_xref="taxon:1056511"
     gene            1..390
                     /gene="prpC"
     Protein         1..390
                     /product="bifunctional 2-methylcitrate synthase/citrate
                     synthase"
                     /EC_number="2.3.3.16"
                     /EC_number="2.3.3.5"
                     /GO_function="GO:0004108 - citrate (Si)-synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050440 - 2-methylcitrate synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0019679 - propionate metabolic process,
                     methylcitrate cycle [Evidence IEA]"
                     /calculated_mol_wt=42986
     Region          18..389
                     /region_name="PRK12351"
                     /note="methylcitrate synthase; Provisional"
                     /db_xref="CDD:183463"
     Site            order(23..25,28..32,94..95,98..99,107,111,115,118,164,
                     201..205,208..209,213,216..219,222,229..230,232..235,276,
                     367..377)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99861"
     Site            order(26,201,204,235..237,239,242,269..276,279,284,319,
                     321,324,326,347,351,367,370)
                     /site_type="active"
                     /db_xref="CDD:99861"
     Site            order(26,201,204,235..236,269..270,272..276,284,324,351)
                     /site_type="other"
                     /note="citrylCoA binding site [chemical binding]"
                     /db_xref="CDD:99861"
     Site            order(201,204,236..237,275,284,326,347,351,370)
                     /site_type="other"
                     /note="oxalacetate/citrate binding site [chemical
                     binding]"
                     /db_xref="CDD:99861"
     Site            order(235..236,239,242,269..274,276,279,319,321,324,326,
                     367)
                     /site_type="other"
                     /note="coenzyme A binding site [chemical binding]"
                     /db_xref="CDD:99861"
     Site            order(236,275,326)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:99861"
ORIGIN      
        1 mtaiavadkk kdnslnnkpl ggaglrgqsa gvtalctvgk tgtgltyrgy ditdlakhae
       61 feevaylllk gklptqaeld sykqalkear glppalcqvl eaipadahpm dvmrtgcsml
      121 gnldqeqdfs eqwektdill amlpaiicyw yryshdgiri dtansgqdsi ggyflemltg
      181 kapselhkqv mhcslvlyae hefnastfta rvcastlsdl hscitaaigs lrgplhggan
      241 eaamamieqw qtsdeaeagi lqmleqkeki mgfghaiyre sdprnalika wseklskdvg
      301 dttlyavser veqvmkrekg lfcnadffha sayhfmgipt klftpifvms rvtgwaahvy
      361 eqrannriir psadytgpeh qewlpieqrs